ライフサイエンスコーパス: misfold

1 uated at variable distances from the site of misfold.

2 ations might predispose PrP to spontaneously misfold.

3 ns and the deleterious consequences of their misfolding.

4 nformation, with no evidence for large-scale misfolding.

5 ns and the end product of pathologic protein misfolding.

6 ases associated with cell stress and protein misfolding.

7 cally, thereby potentiating slow folding and misfolding.

8 degradation in the knock-in mouse RPE due to misfolding.

9 oluble under conditions that promote protein misfolding.

10 g protein homeostasis and preventing protein misfolding.

11 nd neurobiological defects caused by protein misfolding.

12 anism that chaperones may exploit to prevent misfolding.

13 n, possibly due to increased cotranslational misfolding.

14 d by poor solubility, low yield, and protein misfolding.

15 follows a seeding-nucleation model, where a misfolded aggregate or 'seed' promotes the rapid misfold

16 tients with type 2 diabetes (T2D) accumulate misfolded aggregates composed of the islet amyloid polyp

17 that PINK1 recruits Parkin proximal to focal misfolded aggregates of the mitochondrial-localized muta

18 es from a "donor cell" that is the source of misfolded aggregates to an "acceptor cell" in which misf

19 hin the exon1 of huntingtin leads to protein misfolding, aggregation, and cytotoxicity in Huntington'

20 elling evidence supports the hypothesis that misfolded alpha-syn transmits from neuron-to-neuron and

21 The notion that prion-like spreading of misfolded alpha-synuclein (alpha-SYN) causes Parkinson's

22 Cell-to-cell spreading of misfolded alpha-synuclein (alpha-syn) is suggested to co

23 Misfolded alpha-synuclein (alphaS) is hypothesized to sp

24 Parkinson's disease (PD) patients accumulate misfolded alpha-synuclein in LBs, the diagnostic signatu

25 mulate intracytoplasmic inclusions formed by misfolded alpha-synuclein known as Lewy bodies (LBs).

26 Extending our findings, we show that misfolding also occurs for IL-23alpha, another IL-12 fam

27 to interfere with aggregation of particular misfolded amyloid peptides or proteins.

28 ivity wherein these MDPs specifically target misfolded amyloid seeds to inhibit IAPP misfolding which

29 Alzheimer's disease (AD) is accumulation of misfolded amyloid-beta peptides and hyperphosphorylated

30 own to yield qualitatively different, highly misfolded amyloid-like fibrils.

31 span variable distances between the site of misfold and a glucose-accepting N-linked glycan on the s

32 fibril formation, amyloidogenic polypeptides misfold and self assemble into soluble pre-fibrillar agg

33 in postmortem brains by the presence of key misfolded and aggregated disease proteins, but cellular

34 Misfolded and aggregated forms of tau produce pathologic

35 ization of the folded state and formation of misfolded and aggregated species.

36 tions: properly folded and non-infectious or misfolded and infectious.

37 vely sort biosynthetic cargo from diffusible misfolded and resident ER proteins.

38 The [PSI(+)] yeast prion, which is the misfolded and self-propagating form of the translation t

39 agents that specifically bind and neutralize misfolded and toxic superoxide dismutase 1 (SOD1) mutant

40 hypotheses and provided evidence for protein misfolding and aberrant target recognition as the underl

41 The misfolding and accumulation of alpha-synuclein (alphaS)

42 ke all membrane proteins, ssMPs are prone to misfolding and aggregation because of the hydrophobicity

43 Cells respond to protein misfolding and aggregation in the cytosol by adjusting g

44 alpha-Synuclein misfolding and aggregation is a hallmark in Parkinson's

45 Protein misfolding and aggregation is increasingly being recogni

46 rodegenerative diseases are characterized by misfolding and aggregation of an expanded polyglutamine

47 t pancreatic IAPP aggregates can promote the misfolding and aggregation of endogenous IAPP in islet c

48 Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo

49 This expansion leads to misfolding and aggregation of mutant ataxin-3 (ATXN3) an

50 uIC technique is based on prion seed-induced misfolding and aggregation of recombinant prion protein

51 olded aggregate or 'seed' promotes the rapid misfolding and aggregation of the native protein.

52 e of these modifications in inducing protein misfolding and aggregation was determined by inducing ca

53 eurodegenerative disorders caused by protein misfolding and aggregation, including amyotrophic latera

54 P23H-1 rat retina, suggesting enhanced P23H misfolding and aggregation.

55 ostasis (proteostasis), resulting in protein misfolding and aggregation.

56 operty was selected by evolution to minimize misfolding and aggregation.

57 sical properties of proteins associated with misfolding and aggregation.

58 ssociated with hyperglycemia-induced protein misfolding and Caspase-8-induced programmed cell death.

59 pansion in the Htt protein, resulting in Htt misfolding and cell death.

60 ing network to study the folding, unfolding, misfolding and conformational plasticity of the high-eff

61 hERG) potassium channel, many of which cause misfolding and degradation at the endoplasmic reticulum

62 tion and biological activity of IL-12 versus misfolding and degradation of IL-12alpha.

63 The clear link between protein misfolding and disease highlights the need to better und

64 sense variants in EHMT1 that lead to protein misfolding and disrupted histone mark binding can lead t

65 gle cause of RP in the USA, causes rhodopsin misfolding and induction of the unfolded protein respons

66 ve slowly because of selection against toxic misfolding and misinteractions, linking their rate of ev

67 rface that becomes exposed upon mutated SOD1 misfolding and monomerization.

68 ctance regulator (CFTR) anion channel causes misfolding and premature degradation.

69 on the molecular factors involved in protein misfolding and the development of ultrasensitive methods

70 Co-expression of its beta subunit inhibits misfolding and thus allows secretion of biologically act

71 s qualitatively different aspects of protein misfolding and toxicity via different quaternary structu

72 er potential triggers of the alpha-synuclein misfolding and why the aggregates escape cellular degrad

73 ent hypothesis is that hyperphosphorylation, misfolding, and fibrillization of tau impair synaptic pl

74 ular perspective on cotranslational folding, misfolding, and the impact of translation speed on these

75 t make rabbit recombinant PrP susceptible to misfolding, and using these, protease-resistant misfolde

76 ms underlying the pathological properties of misfolding- and aggregation-prone proteins remain a chal

77 f cellular compartments to cytosolic protein misfolding are less clear.

78 rescence studies show that HNG inhibits IAPP misfolding at highly substoichiometric concentrations.

79 lating SAA is protected from proteolysis and misfolding by binding to plasma high-density lipoprotein

80 tients with variant CJD (vCJD) using protein misfolding by cyclic amplification, which was apparently

81 proposed to exert protective effects against misfolding by interfering with eIF2alpha-P dephosphoryla

82 Protein misfolding caused by inherited mutations leads to loss o

83 imaging methods and genetic show that Al(3+) misfolds cell membrane proteins, while Fe(2+) evokes mem

84 p.Phe508del, results in the production of a misfolded CFTR protein, which has residual channel activ

85 ative disorder caused by prion protein (PrP) misfolding, clinically recognized by cognitive and motor

86 n, CBZ application stimulated proteolysis of misfolded collagen X by either autophagy or proteasomal

87 tructural transitions between a native and a misfolded conformation and simulate their synthesis by t

88 The self-propagation of misfolded conformations of tau underlies neurodegenerati

89 iates, decreasing the likelihood of sampling misfolded conformations.

90 ional selection step, proteins often display misfolded conformations.

91 Here, we optimized the protein misfolding cyclic amplification (PMCA) assay for highly

92 d a prion conversion in vitro assay, protein misfolding cyclic amplification (PMCA), by using experim

93 sceptibility to PrP(Sc) propagation, protein misfolding cyclic amplification (PMCA), which mimics PrP

94 We further demonstrated protein misfolding cyclic amplification (PMCA)-competent prions

95 protein amplification assays-such as protein misfolding cyclic amplification (PMCA)-which are based o

96 An adapted Protein Misfolding Cyclic Amplification methodology based on the

97 Horse prions produced in vitro by protein misfolding cyclic amplification of mouse prions using ho

98 ed control PrP(Sc) from PrP(C) using protein misfolding cyclic amplification with beads (PMCAb), and

99 In contrast, Nrf2 sequestered misfolded diffuse LRRK2 into more insoluble and homogene

100 used for the investigation of other protein misfolding diseases such as Alzheimer's and Parkinson's

101 r homeostasis can be deteriorated in protein misfolding diseases.

102 pathologic states that are viewed as protein-misfolding diseases.

103 to development into therapeutics for protein-misfolding diseases.

104 g target for modifying the course of protein misfolding diseases.

105 Huntington's disease (HD) and other protein misfolding diseases.

106 to improve protein function in other protein misfolding diseases.

107 Both diseases are considered protein misfolding disorders associated with the accumulation of

108 ents for prion diseases and possibly protein misfolding disorders involving prion-like mechanisms.

109 has important implications for human protein misfolding disorders.

110 pathies that are collectively termed protein misfolding disorders.

111 2D and AD, two of the most prevalent protein misfolding disorders.

112 ection, monitoring and treatment of multiple misfolding disorders.

113 Proteins with misfolded domains in the endoplasmic reticulum lumen or

114 aggregated reporter polypeptides as well as misfolded endogenous proteins inside mitochondria takes

115 Misfolded endoplasmic reticulum proteins are retro-trans

116 serve as a clinical example of the effect of misfolded ER proteins retrotranslocated through the memb

117 essive neurodegenerative disorders caused by misfolding followed by aggregation and accumulation of p

118 rafts in which conversion to the pathogenic misfolded form is believed to occur.

119 the peculiarity of the pathogen, which is a misfolded form of a normal protein.

120 es, characterized by the accumulation of the misfolded form of the prion protein, which is followed b

121 the uromodulin (UMOD) gene that result in a misfolded form of UMOD protein, which is normally secret

122 s to form its native structure but, instead, misfolds, forming incorrect disulfide bonds.

123 tors and identify diagnostic markers for the misfolded forms identified here.

124 rent location, were treated with infectious, misfolded forms of the prion protein, PrP(res) We show t

125 hat this growth defect may be due in part to misfolded FtsN.

126 mechanisms underlying the link among genome misfolding, genome dysregulation, and aberrant cellular

127 ns remain on how this single enzyme can flag misfolded glycoproteins of different sizes and shapes fo

128 ol checkpoint: it selectively reglucosylates misfolded glycoproteins, promotes their association with

129 Here we analyzed the degradation of the misfolded GPI-AP Gas1* in yeast.

130 Proteins begin to fold in the ribosome, and misfolding has pathological consequences.

131 TRC8 also mediates degradation of the misfolded hERG-G601S disease mutant, but pharmacological

132 plicating the challenges of neuroprotection, misfolded human disease proteins and mitochondria can mo

133 Here, we examined how misfolded IAPP affects Abeta aggregation and AD patholog

134 Our underlying hypothesis is that misfolded IAPP produced in T2D potentiates AD pathology

135 unction and muscle wasting caused by protein misfolding in HD.

136 Moreover, proAVP misfolding in hereditary central diabetes insipidus like

137 hysiopathological mechanisms with proinsulin misfolding in hereditary diabetes mellitus of youth.

138 sign as well as defining the role of protein misfolding in neurodegenerative disorders.

139 nsitive antibody, TNT2, to determine whether misfolding in the amino terminus (ie, PAD exposure) occu

140 rPres, which was the first product of PrP(C) misfolding in vivo.

141 to prion diseases) and the study of protein misfolding; in addition, it can potentially be used for

142 of ApoE4 by preventing the formation of the misfolded intermediate state.

143 ve identified a structural model of an ApoE4 misfolded intermediate state.

144 protein folding, where partial unfolding of misfolded intermediates plays a key role.

145 lational protein folding by helping to avoid misfolded intermediates.

146 , tau, alpha-synuclein, and serum amyloid A, misfold into distinct conformers linked to different cli

147 ild-type rabbit recombinant PrP could not be misfolded into a protease-resistant self-propagating iso

148 the prion protein (PrP(C)) influences PrP(C) misfolding into the disease-associated isoform, PrP(res)

149 r's disease the amyloid-beta peptide (Abeta) misfolds into neurotoxic oligomers and assembles into am

150 Protein misfolding is a common hypothesis underlying the develop

151 Protein misfolding is a key pathological event in neurodegenerat

152 Misfolding is believed to be mediated by both the N- and

153 n emerging model in which genome folding and misfolding is critically linked to the onset and progres

154 lement (TAR) DNA-binding protein 43 (TDP-43) misfolding is implicated in several neurodegenerative di

155 Protein misfolding is linked to a rapidly expanding list of huma

156 olding mechanism, we find that the extent of misfolding is not determined by the relative folding rat

157 ed aggregates to an "acceptor cell" in which misfolding is propagated by conversion of the normal pro

158 Protein misfolding is toxic to cells and is believed to underlie

159 on is attributed to PrP-scrapie (PrP(Sc)), a misfolded isoform of prion protein (PrP(C)) that accumul

160 hies, characterized by the accumulation of a misfolded isoform of the host cellular prion protein (Pr

161 Its misfolded isoform PrP(Sc) is the causative agent of prio

162 d that the latter would have a propensity to misfold, leading to abnormal histone mark binding.

163 MYOC mutations result in protein misfolding, leading to endoplasmic reticulum (ER) stress

164 We hypothesised that the ability of p17 to misfold may result in the generation of toxic assemblies

165 To unveil the protein misfolding mechanism and to understand why some mutation

166 y expected based on the previously described misfolding mechanism, we find that the extent of misfold

167 euronal stress including the accumulation of misfolded mHTTx1.

168 s range from various types of aggregates to "misfolded" monomers.

169 ed chains and identified mitotic regulators, misfolded nascent polypeptides, and pathological Hunting

170 Once misfolding occurs, the pathogenic isoform polymerizes in

171 , where one aggregated protein templates the misfolding of a heterologous protein, is one mechanism p

172 Here, we show that misfolding of ALS-linked SOD1 mutants and wild-type (wt)

173 In vitro, the compounds induce misfolding of chromatin fibre and block the binding of t

174 small humanin-like peptide 2 (SHLP2), on the misfolding of islet amyloid polypeptide (IAPP), a critic

175 Misfolding of mutant FUS is implicated in this process,

176 The misfolding of proteins and their accumulation in extrace

177 gen species, protein chaperones that prevent misfolding of proteins, and proteases that degrade toxic

178 Misfolding of tau proteins into prions and their propaga

179 llagen, which increase ER stress by inducing misfolding of the mutant protein and subsequently disrup

180 Introducing the mutation does not cause misfolding of the SH3 domains, but abolishes the interac

181 Misfolding, oligomerization and accumulation of the huma

182 n conjunction with the proteasome to degrade misfolded or damaged proteins.

183 membrane proteins and secretory proteins are misfolded or incompletely folded, they are retained in t

184 provide a chaperone-like activity to prevent misfolding or aggregation as the preprotein traverses th

185 have the proteins they need while minimizing misfolding or aggregation events that are hallmarks of a

186 werful approaches to dissect the complicated misfolding pathways of protein aggregation.

187 ro-translocation channel for the movement of misfolded polypeptides through the endoplasmic reticulum

188 ) may be due to cell-to-cell transmission of misfolded preformed fibrils (PFF) of alpha-synuclein (al

189 Misfolded prion protein aggregates (PrP(Sc)) show remark

190 Prions are unconventional agents composed of misfolded prion protein that cause fatal neurodegenerati

191 n (ERAD) is responsible for the clearance of misfolded pro-arginine vasopressin (proAVP) in the ER.

192 predictions, we find that rapid synthesis of misfolding-prone nascent-chain segments increases the fr

193 tions in rabbit PrP and accurate analysis of misfolding propensities.

194 rs caused by prions, which are composed of a misfolded protein (PrP(Sc)) that self-propagates in the

195 oteasome system (UPS) to avoid a build-up of misfolded protein aggregates.

196 In contrast to other in vitro misfolded protein amplification assays-such as protein m

197 pathway senses influenza HA as "nonself" or misfolded protein and sorts HA to ERAD for degradation,

198 urodegenerative diseases are associated with misfolded protein assemblies called amyloid.

199 e recognized as nonself by immune receptors, misfolded protein assemblies evade detection, as they ar

200 o decrease the intracellular accumulation of misfolded protein may be successful in some patients wit

201 so provide a basis for understanding how the misfolded protein structure impacts the disease.

202 tin ligases append polyubiquitin chains onto misfolded protein substrates signaling for their degrada

203 29) mutation to glutamate or arginine led to misfolded protein that was degraded in vivo Mutation to

204 id receptor and degradation of a permanently misfolded protein, two previously defined roles for Sse1

205 ion machinery, or because of toxicity of the misfolded protein.

206 itro under stress conditions, including when misfolded proteins accumulate.

207 ing mechanisms to reduce the accumulation of misfolded proteins an attractive therapeutic strategy.

208 le-dependent inclusion bodies that sequester misfolded proteins and are ultimately removed by autopha

209 halose in studies of autophagic clearance of misfolded proteins and for targeting SGs as a possible t

210 The toxicity of misfolded proteins and mitochondrial dysfunction are piv

211 ins that can reduce the cellular toxicity of misfolded proteins and prevent neurodegeneration.

212 Misfolded proteins are associated with many human diseas

213 COPII-coated vesicles, whereas resident and misfolded proteins are substantially excluded from vesic

214 The present study shows that misfolded proteins are ubiquitinylated, suggesting that

215 racterized pathologically by accumulation of misfolded proteins as a result of gene mutations or abno

216 characterized by extracellular deposition of misfolded proteins as insoluble fibrils.

217 ew the proposed mechanisms whereby exemplary misfolded proteins associate with mitochondria and their

218 Misfolded proteins associate with mitochondria, forming

219 for the degradation of chaperone-associated misfolded proteins by the ubiquitin-proteasome system.

220 uring development as well as many neurotoxic misfolded proteins during pathogenesis.

221 quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD).

222 Misfolded proteins form aggregates containing ubiquitin-

223 regulatory proteins and removes damaged and misfolded proteins from cells.

224 ocalizes on polarized mitochondria harboring misfolded proteins in foci with ubiquitin, optineurin, a

225 ses are characterized by the accumulation of misfolded proteins in intra- and extracellular inclusion

226 tion in vitro, prevented the accumulation of misfolded proteins in living cells, and reduced the cyto

227 thway facilitates the disposal of terminally misfolded proteins in the early secretory pathway yet sp

228 culum (ER) stress causes the accumulation of misfolded proteins in the ER, activating the transcripti

229 which protects cells against accumulation of misfolded proteins in the ER, is induced in several age-

230 stress is brought on by the accumulation of misfolded proteins in the ER, which leads to activation

231 lum (ER) localized endonuclease activated by misfolded proteins in the ER.

232 Soon thereafter, a distinct UPRmt induced by misfolded proteins in the mitochondrial intermembrane sp

233 nvolve the damaging accumulation of specific misfolded proteins in thread-like aggregates.

234 cytosolic Hsp70s leads to enhanced entry of misfolded proteins into mitochondria and elevated mitoch

235 for this pathway, and the failure to destroy misfolded proteins is associated with a number of human

236 integral part of the cellular management of misfolded proteins is their spatial sequestration into s

237 expression of chaperones that refold damaged misfolded proteins or facilitate their degradation.

238 Misfolded proteins represent an important class of subst

239 ecPMCA) generated different self-propagating misfolded proteins spontaneously.

240 nes similarly to the aggregation of toxic or misfolded proteins such as those associated with Parkins

241 for the proteasomal degradation of cytosolic misfolded proteins targeted by Rsp5 after heat-shock (HS

242 s binding Nt-Arg and other N-degrons.Soluble misfolded proteins that fail to be degraded by the ubiqu

243 sease mechanism involving the interaction of misfolded proteins through cross-seeding events which ma

244 on of J-domains of transferring unfolded and misfolded proteins to Hsp70.

245 ms to enhance the folding and degradation of misfolded proteins to restore proteostasis.

246 Accumulation of misfolded proteins triggers endoplasmic reticulum stress

247 AD) machinery efficiently targets terminally misfolded proteins while avoiding the misidentification

248 which uses EVs as vehicles for immature and misfolded proteins, forming circulating immune complexes

249 esponse to the accumulation of aggregates of misfolded proteins, known as aggresomes.

250 pe with stress and increased accumulation of misfolded proteins, plants and animals use a survival pa

251 ionally, it degrades abnormal/damaged/mutant/misfolded proteins, which serves a quality-control funct

252 ies are characterized by the accumulation of misfolded proteins, which ultimately interfere with norm

253 12 has been shown to facilitate clearance of misfolded proteins.

254 romoting ER-associated degradation (ERAD) of misfolded proteins.

255 tress-induced degradation and aggregation of misfolded proteins.

256 have developed stress responses to deal with misfolded proteins.

257 ght control of partitioning and recycling of misfolded proteins.

258 ER in DYT1 mice by increasing the amount of misfolded proteins.

259 drome, which arise from transport defects of misfolded proteins.

260 thereby enables refolding or degradation of misfolded proteins.

261 ated distinct mechanisms to handle different misfolded proteins.

262 other diseases involving the accumulation of misfolded proteins.

263 ch defects are caused by the accumulation of misfolded proteins.

264 stingly, the proteases involved in resolving misfolded Psd1(ts) vary depending on its autocatalytic s

265 onships reflect the implicit threat of toxic misfolding (rather than hormonal function at the recepto

266 tense scrutiny however, the mechanism of the misfolding reaction remains unclear.

267 folding, and using these, protease-resistant misfolded recombinant rabbit PrP was generated.

268 The early stages of protein misfolding remain incompletely understood, as most mamma

269 e data suggest that improving the traffic of misfolding rhodopsin mutants is unlikely to be a practic

270 dence supports transcellular transfer of tau misfolding (seeding) as the mechanism of spread within a

271 MDPs block amyloid seeding and directly bind misfolded, seeding-capable IAPP species.

272 teinaceous infectious agents that consist of misfolded, self-replicating states of a sialoglycoprotei

273 defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus.

274 ecognizes this NES-like sequence and exports misfolded SOD1 to the cytoplasm.

275 dies against the NES-like sequence recognize misfolded SOD1, but not native wt SOD1 both in vitro and

276 Metastable proteins tend to populate misfolded species that are prone to forming toxic aggreg

277 ing and leads to efficient ER export of even misfolded species.

278 n two biophysical properties of the client's misfolded state (M state): its stability and its kinetic

279 dysfunctions have been linked to this ApoE4 misfolded state.

280 res, three intermediate states, and numerous misfolded states, the latter of which have not previousl

281 by the R61T mutation in the ApoE4 native and misfolded states.

282 t NAC can protect astrocytes against protein misfolding stress (proteotoxicity), the hallmark of neur

283 Their analysis is based on a partially misfolded structure of the iron-sulfur cluster domain of

284 e initial intermediates leading to folded or misfolded structures.

285 Unassembled and misfolded subunits undergo ER-associated degradation (ER

286 ino acid residue substitutions increased the misfolding susceptibility of rabbit PrP.IMPORTANCE Prion

287 Here, we show that when misfolded tau assemblies enter the cell, they can be det

288 ated that experimentally propagated forms of misfolded tau can exist as conformationally distinct "st

289 dies in cell and animal models revealed that misfolded tau can propagate from cell to cell and from r

290 d within the last decade to suggest that the misfolded tau in tauopathies possesses prion-like featur

291 pathies may be a reflection of the strain of misfolded tau that propagates in each disease.

292 PrP(C) misfolds to a pathogenic isoform PrP(Sc), the causative

293 Nanomolar misTTR inhibits fibrillogenesis of misfolded TTR under micromolar concentrations.

294 ulum (ER) stress arises from accumulation of misfolded/unfolded proteins when protein load overwhelms

295 Here, we introduce a protocol to incorporate misfolding using the functional forms of publicly availa

296 tion of natively folded and mutation-induced misfolded von Willebrand disease (VWD) variants, we test

297 rget misfolded amyloid seeds to inhibit IAPP misfolding which, along with direct anti-apoptotic activ

298 to refold and their increased propensity to misfold, which makes them vulnerable to large thermal fl

299 Point mutations in SLC6 transporters cause misfolding, which can be remedied by pharmacochaperones.

300 pe of conformational disorder due to protein misfolding with consequent aberrant intermolecular prote